Skip to main content
. Author manuscript; available in PMC: 2012 Oct 19.
Published in final edited form as: J Am Chem Soc. 2011 Sep 28;133(41):16428–16431. doi: 10.1021/ja208019p

Figure 3.

Figure 3

Proposed free energy profiles for the turnover of glycolaldehyde (S) by free TIM (Eo) and by the phosphite-liganded enzyme Ec•HPO32-. The red bars show the effect of the L232A mutation on the barrier for the conformational change from Eo to Ec (ΔΔGc). The effect of this change in ΔGc on turnover of the substrate pieces is shown by a comparison of the reaction profiles for wildtype TIM (upper dashed lines) and L232A mutant TIM (lower dashed lines).